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Very interesting but completely false.
I am a R&D biochemist. While many of the igf peptides sold online are fake or are less than 70% pure, some are real. Get them tested , reverse phase hplc and page electrophoresis.
synthetic igf will bind as well as that which is bio synthesized (rDNA)
the most important test is binding affinity, how much of the peptide actually binds to the receptor.
Also,any peptide over 60 amino acids long is not feasible by solid phase synthesis , only recombinant DNA using bacteria can efficiently achieve this.
Please check your science before making assumptions or uneducated guesses.
[h=3]Abstract[/h]Insulin-like growth factor-1 (IGF-1), whether recombinant, chemically-synthesised or purified from bovine colostrum, was equipotent in radioreceptor assays with IGF-1 or insulin-like growth factor-2 (IGF-2) as radioligand as well as in its ability to stimulate protein synthesis in L6 myoblasts. The N-terminal truncated, destripeptide derivative of IGF-1 was approximately 7 times more potent than IGF-1 in the protein synthesis bioassay. This increased activity occurred equally with the peptide purified from bovine colostrum as with chemically-synthesised material. The higher potency of the truncated form was not associated with an increased ability to compete for IGF-1 binding to L6 myoblasts.
I am a R&D biochemist. While many of the igf peptides sold online are fake or are less than 70% pure, some are real. Get them tested , reverse phase hplc and page electrophoresis.
synthetic igf will bind as well as that which is bio synthesized (rDNA)
the most important test is binding affinity, how much of the peptide actually binds to the receptor.
Also,any peptide over 60 amino acids long is not feasible by solid phase synthesis , only recombinant DNA using bacteria can efficiently achieve this.
Please check your science before making assumptions or uneducated guesses.
[h=3]Abstract[/h]Insulin-like growth factor-1 (IGF-1), whether recombinant, chemically-synthesised or purified from bovine colostrum, was equipotent in radioreceptor assays with IGF-1 or insulin-like growth factor-2 (IGF-2) as radioligand as well as in its ability to stimulate protein synthesis in L6 myoblasts. The N-terminal truncated, destripeptide derivative of IGF-1 was approximately 7 times more potent than IGF-1 in the protein synthesis bioassay. This increased activity occurred equally with the peptide purified from bovine colostrum as with chemically-synthesised material. The higher potency of the truncated form was not associated with an increased ability to compete for IGF-1 binding to L6 myoblasts.